ID A0AAQ6IBF6_ANATE Unreviewed; 1270 AA.
AC A0AAQ6IBF6;
DT 27-NOV-2024, integrated into UniProtKB/TrEMBL.
DT 27-NOV-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000074220.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000074220.1, ECO:0000313|Proteomes:UP000265040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSATEP00000074220.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSATEP00000074220.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_026231299.1; XM_026375514.1.
DR AlphaFoldDB; A0AAQ6IBF6; -.
DR Ensembl; ENSATET00000077552.1; ENSATEP00000074220.1; ENSATEG00000030413.1.
DR GeneID; 113172517; -.
DR CTD; 558137; -.
DR GeneTree; ENSGT00940000164061; -.
DR Proteomes; UP000265040; Chromosome 17.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1270
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043994930"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..353
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..640
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..720
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..832
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..888
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..968
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1053
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 130636 MW; F2BA67496FA33E25 CRC64;
MFQRWCLVLH LVLLRWLAAA HQVTEDQGSG DHLDLMELIG VPLPPSVSFS PGYDDFPAYN
FGPEANIGRL TKTFVPGSFY RDFAIIVTVR PASQRGGVLF AITDARQKVV ELGLALTPVS
EGLQSILLYY TDSHHASHSH KAAAFSVSDM TDQWTRFTVA VEHDEVRLYM DCGEPERATF
QRRAGKLTFS HNSGIFVANA GSTGLDKFVG SIEQLVIKDD PRAAEEQCED DDPYASGYAS
GDDGLDDRET EEEKAKNAQE RKEENSAPVR APPTEIPEVE LNEYSGRMTP TEAYEEMLTR
GPHQTEEPGK RSEDRNFRPE LKGEPGDAGP PGPPGPPGPT PVPGHAQPGQ TEPQGPPGVP
GSPGQPGTDG RQGSKGDKGD LGQRGPRGFP GLDGTPGTKG EKGDLGVGLP GPPGLPGPPG
PPRSRSVPYG ADALGSGFED VDTDSELIRG PPGPPGPPGP PGPPGTNLSS SATAGGLVPG
HAGPPGAPGK DGLPGQPGIP GPAGKDGAPG LPGPVGEKGD QGLPGPSGPK GECGAEGRAG
PSGPQGPTGP QGERGPIGPP GPPGPPGPPG PPRTNFFAED MEGSGKNDML IGAGARGPQG
PTGLPGPQGP KGDDGAPGAP GLSVKGEPGI PGPHGIQGPA GLPGPRGAKG EKGSPGPKGD
HGVDGLSIPG PPGPPGPPGP MINLQDLLLN VTDGVFNFSE IRGPPGPIGP EGLPGRAGFP
GPRGPKGDRG LPGVQGPSGH KGEKGEPGVT IAADGSILSA PRGPQGPKGI KGDRGFPGPL
GHMGPIGPTG QKGEYGFPGR PGRPGMPGRK GDKGDAVGLP GPPGPPGPPG PPGRILGLNG
TVFPVRPRPH CKKGRESETR EDSVGVKGDK GDQGTPGEPG TPTAPGFPEV IVGARGDQGY
KGQKGEKGDA APPGPPGLPG RSGLVGPKGE SIMGPPGPVG SPGLPGAPGF GQPGPRGPPG
PAGPPGPAPA YESAVNIPGP PGPPGPPGSP GDPVTAYITV HYLPREAEEG SLAYVSERGG
ELYVRTQKGW RMIQLGELIP HDPSSSPVSQ ASSRPEEWSR PHRIHSQELH EGRRGYQPSY
NVLPQTFNAV PGLHLVALNA PLKGDMRGIR GADFQCYQQA RSMGLTATYR AFLSSHLQDL
ATIVRKADRN DMPVVNLRGE VLFSSWMSIF SGNGGMFNPS TPIYSFDGRN IMTDPAWPEK
LVWHGSSTVG IRLTTNYCEA WRTADMAVTG QAALLQTGRL LGQHTRSCSN HYIVLCIENT
YVGNTHPRRP
//
